Localization of a gene controlling the expression of the human transferrin receptor to the region q12→qter of chromosome 3

1983 ◽  
Vol 36 (3) ◽  
pp. 525-531 ◽  
Author(s):  
M. van de Rijna ◽  
A.H.M. Geurts van Kessel ◽  
V. Kroezen ◽  
A.J. van Agthoven ◽  
K. Verstijnen ◽  
...  
Keyword(s):  
Transferrin Receptor ◽  
Chromosome 3 ◽  
Human Transferrin ◽  
Human Transferrin Receptor

scholarly journals Human transferrin receptor: expression of the receptor is assigned to chromosome 3.

1982 ◽  
Vol 79 (10) ◽  
pp. 3241-3245 ◽  
Author(s):  
C. A. Enns ◽  
H. A. Suomalainen ◽  
J. E. Gebhardt ◽  
J. Schroder ◽  
H. H. Sussman
Keyword(s):  
Transferrin Receptor ◽  
Receptor Expression ◽  
Chromosome 3 ◽  
Human Transferrin ◽  
Human Transferrin Receptor ◽  
Transferrin Receptor Expression

scholarly journals Structural model of phospholipid-reconstituted human transferrin receptor derived by electron microscopy

Structure ◽  
1998 ◽  
Vol 6 (10) ◽  
pp. 1235-1243 ◽  
Author(s):  
Hendrik Fuchs ◽  
Uwe Lücken ◽  
Rudolf Tauber ◽  
Andreas Engel ◽  
Reinhard Geßner
Keyword(s):  
Electron Microscopy ◽  
Transferrin Receptor ◽  
Structural Model ◽  
Human Transferrin ◽  
Human Transferrin Receptor

The Promoter Region of the Human Transferrin Receptor Gene

1988 ◽  
Vol 526 (1 Hemochromatos) ◽  
pp. 54-64 ◽  
Author(s):  
John L. Casey ◽  
Bruno Jeso ◽  
Krishnamurthy Rao ◽  
Tracey A. Rouault ◽  
Richard D. Klausner ◽  
...  
Keyword(s):  
Transferrin Receptor ◽  
Promoter Region ◽  
Receptor Gene ◽  
Human Transferrin ◽  
Human Transferrin Receptor

scholarly journals Human transferrin receptor internalization is partially dependent upon an aromatic amino acid on the cytoplasmic domain.

1990 ◽  
Vol 1 (4) ◽  
pp. 369-377 ◽  
Author(s):  
T E McGraw ◽  
F R Maxfield
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Rate Constant ◽  
Transferrin Receptor ◽  
Aromatic Amino Acid ◽  
Opposite Polarity ◽  
Receptor Internalization ◽  
Aromatic Side Chain ◽  
Human Transferrin ◽  
Human Transferrin Receptor

The objective of this work is to identify the elements of the human transferrin receptor that are involved in receptor internalization, intracellular sorting, and recycling. We have found that an aromatic side chain at position 20 on the cytoplasmic portion of the human transferrin receptor is required for efficient internalization. The wild-type human transferrin receptor has a tyrosine at this position. Replacement of the Tyr-20 with an aromatic amino acid does not alter the rate constant of internalization, whereas substitution with the nonaromatic amino acids serine, leucine, or cysteine reduces the internalization rate constant approximately three-fold. These results are consistent with similar studies of other receptor systems that have also documented the requirement for a tyrosine in rapid internalization. The amino terminus of the transferrin receptor is cytoplasmic, with the tyrosine 41 amino acids from the membrane. These two features distinguish the transferrin receptor from the other membrane proteins for which the role of tyrosine in internalization has been examined, because these proteins have the opposite polarity with respect to the membrane and because the tyrosines are located closer to the membrane (within 25 amino acids). The externalization rate for the recycling of the transferrin receptor is not altered by any of these substitutions, demonstrating that the aromatic amino acid internalization signal is not required for the efficient exocytosis of internalized receptor.

Identification of the O-linked glycosylation site of the human transferrin receptor

Glycobiology ◽  
1992 ◽  
Vol 2 (4) ◽  
pp. 355-359 ◽  
Author(s):  
Gary R. Hayes ◽  
Caroline A. Enns ◽  
John J. Lucas
Keyword(s):  
Transferrin Receptor ◽  
Glycosylation Site ◽  
Human Transferrin ◽  
Human Transferrin Receptor
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